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Titolo:
ACCESSIBILITY OF PEPTIDES DISPLAYED ON FILAMENTOUS BACTERIOPHAGE VIRIONS - SUSCEPTIBILITY TO PROTEINASES
Autore:
TERRY TD; MALIK P; PERHAM RN;
Indirizzi:
UNIV CAMBRIDGE,DEPT BIOCHEM,CAMBRIDGE CTR MOL RECOGNIT,TENNIS COURT RD CAMBRIDGE CB2 1QW ENGLAND UNIV CAMBRIDGE,DEPT BIOCHEM,CAMBRIDGE CTR MOL RECOGNIT CAMBRIDGE CB2 1QW ENGLAND
Titolo Testata:
Biological chemistry
fascicolo: 6, volume: 378, anno: 1997,
pagine: 523 - 530
SICI:
1431-6730(1997)378:6<523:AOPDOF>2.0.ZU;2-3
Fonte:
ISI
Lingua:
ENG
Soggetto:
LIMITED PROTEOLYTIC SITES; PHAGE DISPLAY; MULTIPLE DISPLAY; FOREIGN PEPTIDES; COAT PROTEIN; LIBRARIES; FD; RECOGNITION; SELECTION; SURFACES;
Keywords:
EPITOPES; GENE MANIPULATION; IMMUNOGENICITY; PEPTIDE LIBRARIES; PHAGE DISPLAY; VACCINES;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
T.D. Terry et al., "ACCESSIBILITY OF PEPTIDES DISPLAYED ON FILAMENTOUS BACTERIOPHAGE VIRIONS - SUSCEPTIBILITY TO PROTEINASES", Biological chemistry, 378(6), 1997, pp. 523-530

Abstract

The genome of the filamentous bacteriophage fd has been engineered sothat small peptides can be inserted into the exposed N-terminal segment of pVIII, the major protein of the virus capsid. Most small peptides can be displayed on all 2700 copies of pVIII (a recombinant virion),but larger peptides can be displayed only in virions in which modified and wild-type proteins are intermingled (hybrid virions). Peptides displayed in this way are highly immunogenic and capable of interactingwith receptors and other ligands. The physical accessibility of the displayed peptides was tested by examining their susceptibility to digestion with proteinases. Potential cleavage sites in peptides displayedon recombinant or hybrid virions were in general found to be accessible to trypsin and chymotrypsin; and the density of incorporation of peptides in the virion had no effect on the susceptibility to cleavage. However, peptide bonds towards the C-terminal end of an insert, located approximately 47 residues or fewer from the C-terminus of the coat protein, were protected from digestion, presumably because of their proximity to the bulk viral surface. These results have important implications for the design and optimization of peptide display systems usingfilamentous bacteriophages.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 16/07/20 alle ore 16:14:23